PMGE_RABIT
ID PMGE_RABIT Reviewed; 259 AA.
AC P07952;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Bisphosphoglycerate mutase;
DE Short=BPGM;
DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P07738};
DE AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte;
DE AltName: Full=2,3-bisphosphoglycerate synthase;
DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P07738};
DE AltName: Full=BPG-dependent PGAM;
GN Name=BPGM;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=3023182; DOI=10.1016/0378-1119(86)90181-2;
RA Yanagawa S., Hitomi K., Sasaki R., Chiba H.;
RT "Isolation and characterization of cDNA encoding rabbit reticulocyte 2,3-
RT bisphosphoglycerate synthase.";
RL Gene 44:185-191(1986).
CC -!- FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity
CC by controlling the levels of its allosteric effector 2,3-
CC bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11)
CC activity. {ECO:0000250|UniProtKB:P07738}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000250|UniProtKB:P07738};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P07738};
CC -!- ACTIVITY REGULATION: At alkaline pH BPGM favors the synthase reaction;
CC however, at lower pH the phosphatase reaction is dominant. Inhibited by
CC citrate. {ECO:0000250|UniProtKB:P07738}.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Expressed in red blood cells.
CC {ECO:0000269|PubMed:3023182}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; M15884; AAA31240.1; -; mRNA.
DR PIR; A24973; PMRBBM.
DR RefSeq; NP_001075738.1; NM_001082269.2.
DR RefSeq; XP_008256342.1; XM_008258120.2.
DR RefSeq; XP_008256343.1; XM_008258121.2.
DR AlphaFoldDB; P07952; -.
DR SMR; P07952; -.
DR STRING; 9986.ENSOCUP00000002728; -.
DR Ensembl; ENSOCUT00000003140; ENSOCUP00000002728; ENSOCUG00000003144.
DR GeneID; 100009096; -.
DR KEGG; ocu:100009096; -.
DR CTD; 669; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P07952; -.
DR OMA; ITESHPY; -.
DR OrthoDB; 1112626at2759; -.
DR TreeFam; TF300007; -.
DR Proteomes; UP000001811; Chromosome 7.
DR Bgee; ENSOCUG00000003144; Expressed in blood and 15 other tissues.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0150076; P:neuroinflammatory response; IEA:Ensembl.
DR GO; GO:0015671; P:oxygen transport; IEA:Ensembl.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT CHAIN 2..259
FT /note="Bisphosphoglycerate mutase"
FT /id="PRO_0000179836"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT SITE 188
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P07738"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07738"
SQ SEQUENCE 259 AA; 30030 MW; 350A0290D24AE528 CRC64;
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL
NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EKMALNHGEE QVRIWRRSYN
VTPPPIEESH PYYHEIYSDR RYRVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG
KTVLISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA
IQAAIKKVED QGKVKRAEK
